Competitive recruitment of CBP and Rb-HDAC regulates UBF acetylation and ribosomal transcription (Q28139506)

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V Y Stefanovsky

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M Faubladier

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I Hirschler-Laszkiewicz

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J Savard

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L I Rothblum

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J Côté

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T Moss

The CBP co-activator is a histone acetyltransferase

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language of work or name

English

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publication date

November 2000

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published in

Molecular Cell

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volume

6

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issue

5

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page(s)

1059-66

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cites work

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Short-range DNA looping by the Xenopus HMG-box transcription factor, xUBF

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Molecular mechanisms governing species-specific transcription of ribosomal RNA

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Retinoblastoma protein recruits histone deacetylase to repress transcription

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Transcriptional role for the nontranscribed spacer of rat ribosomal DNA.

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Activity of RNA polymerase I transcription factor UBF blocked by Rb gene product

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Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation

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The enhancers and promoters of the Xenopus laevis ribosomal spacer are associated with histones upon active transcription of the ribosomal genes.

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Serine15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2.

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Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex

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Nucleotide sequence requirements for specific initiation of transcription by RNA polymerase I

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Amino acid starvation affects the initiation frequency of nucleolar RNA polymerase

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Variants of theXenopus laevisribosomal transcription factor xUBF are developmentally regulated by differential splicing

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Overexpression of the transcription factor UBF1 is sufficient to increase ribosomal DNA transcription in neonatal cardiomyocytes: implications for cardiac hypertrophy

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Regulation of ribosomal DNA transcription by insulin

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Cellular regulation of ribosomal DNA transcription:both rat and Xenopus UBF1 stimulate rDNA transcription in 3T3 fibroblasts

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Histone deacetylase activity is required for full transcriptional repression by mSin3A

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Multiple domains of the RNA polymerase I activator hUBF interact with the TATA-binding protein complex hSL1 to mediate transcription

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Identification of cellular proteins that can interact specifically with the T/ElA-binding region of the retinoblastoma gene product

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Phosphorylation of the rRNA transcription factor upstream binding factor promotes its association with TATA binding protein

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Acetylation: a regulatory modification to rival phosphorylation?

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Dual role of the nucleolar transcription factor UBF: trans-activator and antirepressor

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Control points in eucaryotic ribosome biogenesis

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Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14.

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Adenoviral ElA-associated protein p300 as a functional homologue of the transcriptional co-activator CBP

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Retinoblastoma protein represses transcription by recruiting a histone deacetylase

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xUBF contains a novel dimerization domain essential for RNA polymerase I transcription

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Transcription of mouse rRNA genes by RNA polymerase I: In vitro and in vivo initiation and processing sites

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Analysis of the phosphorylation, DNA-binding and dimerization properties of the RNA polymerase I transcription factors UBF1 and UBF2

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rUBF, an RNA polymerase I transcription factor from rats, produces DNase I footprints identical to those produced by xUBF, its homolog from frogs

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The CREB-binding protein (CBP) cooperates with the serum response factor for transactivation of the c-fos serum response element

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The DNA supercoiling architecture induced by the transcription factor xUBF requires three of its five HMG-boxes

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Recruitment of TATA-binding protein-TAFI complex SL1 to the human ribosomal DNA promoter is mediated by the carboxy-terminal activation domain of upstream binding factor (UBF) and is regulated by UBF phosphorylation

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Activation of mammalian ribosomal gene transcription requires phosphorylation of the nucleolar transcription factor UBF

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Mechanism of repression of RNA polymerase I transcription by the retinoblastoma protein

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Phosphorylation by G1-specific cdk-cyclin complexes activates the nucleolar transcription factor UBF.

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Drosophila CBP represses the transcription factor TCF to antagonize Wingless signalling.

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Chromatin disruption and modification

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Identifiers

DOI

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Fatcat ID

release_q26tjjnp4rfmjbn762r7q3vo5e

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/q26tjjnp4rfmjbn762r7q3vo5e

24 November 2022